Efforts were directed to gaining an atomic level understanding of how the structural parts of a protein carry out its specific function. Proteins were studied by various techniques such as optical, Raman, electron diffraction and steady-state IR. However, these techniques are incapable of directly monitoring the dynamics of the protein backbone. The technique of picosecond infrared difference spectroscopy being developed here with its sensitivity to all parts of the protein and its ultrafast time resolution is hoped to be an invaluable tool for this purpose. As a test bed for this emerging technology we have used bacteriorhodopsin (bR), from the membrane of Halobacterium halobium. Changes of the order of 1part in 10,000 induced by optical excitationinthe absorbance spectrum of bR in the mid infrared (1700 - 1560 cm-1)with a 50 picosecond time resolution were already observed. The protein backbone has pronounced absorption bands in this region that an isomerization of the retinal chromophore and subsequent events in the bR photocycle are expected to perturb. We haverecorded difference spectra from 100 ps to 14 ns. Techniques are now being developed to probe conformational changes in the far-IR and compare these changes with steady-state measurements being performed at the Brookhaven National Laboratories synchrotron.